Analytical Data
-
Gene name
ERP27
- Application
-
Alternative Names
ERP27；C12orf46;Endoplasmic reticulum resident Protein 27
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96DN0
-
Expression Region
26-273aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MEVEKSSDGP GAAQEPTWLT DVPAAMEFIA ATEVAVIGFF QDLEIPAVPI LHSMVQKFPG VSFGISTDSE VLTHYNITGN TICLFRLVDN EQLNLEDEDI ESIDATKLSR FIEINSLHMV TEYNPVTVIG LFNSVIQIHL LLIMNKASPE YEENMHRYQK AAKLFQGKIL FILVDSGMKE NGKVISFFKL KESQLPALAI YQTLDDEWDT LPTAEVSVEH VQNFCDGFLS GKLLKENRES EGKTPKVEL
-
Molecular Weight
30 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ERP27, known as endoplasmic reticulum resident protein 27, is a member of the heat shock protein family and functions as an essential chaperone in the endoplasmic reticulum (ER). Its primary role includes facilitating the proper folding of nascent proteins and mitigating stress responses within the ER, which is crucial for maintaining cellular homeostasis. Recent studies have highlighted the involvement of ERP27 in various physiological and pathological processes, including cancer development and neurodegenerative diseases, suggesting that it may serve as a potential biomarker or therapeutic target. The understanding of ERP27’s structure and function has expanded, revealing insights into its mechanism of action in protein sorting and quality control. Researchers are investigating the regulatory pathways associated with ERP27, as well as its interactions with other proteins, to elucidate its contribution to cellular stress responses and overall protein homeostasis. Given the implications of ER stress in numerous diseases, including diabetes and liver disorders, ERP27's role in modulating these pathways has garnered significant interest in the field of molecular biology and biochemistry, making it a promising candidate for future therapeutic interventions aimed at enhancing ER function and mitigating disease outcomes.
